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Titolo:
BIOCHEMICAL AND FUNCTIONAL-PROPERTIES OF LYSINE-SPECIFIC CYSTEINE PROTEINASE (LYS-GINGIPAIN) AS A VIRULENCE FACTOR OF PORPHYROMONAS-GINGIVALIS IN PERIODONTAL-DISEASE
Autore:
ABE N; KADOWAKI T; OKAMOTO K; NAKAYAMA K; OHISHI M; YAMAMOTO K;
Indirizzi:
KYUSHU UNIV,FAC DENT,DEPT PHARMACOL FUKUOKA 81282 JAPAN KYUSHU UNIV,FAC DENT,DEPT PHARMACOL FUKUOKA 81282 JAPAN KYUSHU UNIV,FAC DENT,DEPT MICROBIOL FUKUOKA 81282 JAPAN KYUSHU UNIV,FAC DENT,DEPT ORAL & MAXILLOFACIAL SURG 1 FUKUOKA 81282 JAPAN
Titolo Testata:
Journal of Biochemistry
fascicolo: 2, volume: 123, anno: 1998,
pagine: 305 - 312
SICI:
0021-924X(1998)123:2<305:BAFOLC>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
ARG-GINGIPAIN; BACTEROIDES-GINGIVALIS; PURIFICATION; PROTEASE; PORPHYPAIN; FORMS;
Keywords:
ARG-GINGIPAIN; LYS-GINGIPAIN; LYSINE-SPECIFIC CYSTEINE PROTEINASE; PERIODONTAL DISEASE; PORPHYROMONAS GINGIVALIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
N. Abe et al., "BIOCHEMICAL AND FUNCTIONAL-PROPERTIES OF LYSINE-SPECIFIC CYSTEINE PROTEINASE (LYS-GINGIPAIN) AS A VIRULENCE FACTOR OF PORPHYROMONAS-GINGIVALIS IN PERIODONTAL-DISEASE", Journal of Biochemistry, 123(2), 1998, pp. 305-312

Abstract

The oral anaerobic bacterium Porphyromonas gingivalis has been implicated as a major etiologic agent of progressive periodontal disease, A novel lysine-specific cysteine proteinase, termed ''Lys-gingipain,'' was purified from the culture supernatant of the Arg-gingipain-deficient mutant of P. gingivalis (KDP112) by a simple method including immunoaffinity chromatography, The purified enzyme was found to be composed of a single polypeptide of M-r=51,000. Analysis of the enzymatic properties revealed several distinctive features of this enzyme. The proteolytic activity was remarkably activated by thiol-reducing agents and inhibited by idoacetamide, idoacetic acid, and leupeptin. The enzyme was also inhibited by the chloromethyl ketones of tosyl-L-lysine and tosyl-L-phenylalanine. However, internal protease inhibitors, such as cystatins and alpha 1-antichymotrypsin, had no effect on the activity, suggesting its resistance to normal host defense systems in. vivo, Despite its narrow specificity for synthetic substrates containing Lys in the P1 site, the enzyme extensively degraded human type I collagen and immunoglobulins G and A (both serum and secretory types). Most important, the enzyme was able to disrupt the functions of polymorphonuclear leukocytes, as shown by its inhibitory effect on the generation of active oxygen species from the activated cells. These results suggest that Lys-gingipain, like Arg-gingipain, plays a crucial role as a virulence factor from P. gingivalis in the development of periodontal diseasevia the direct destruction of periodontal tissue components and the disruption of normal host defense mechanisms.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/11/20 alle ore 20:38:54